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a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
active site structure with bound cofactor, the reduced pyrroloquinoline quinone (PQQ) transfers two electrons in single electron-transfer steps to cytochrome cL, creating a semiquinone form of the prosthetic group after the first electron transfer, electron transfer via enzyme residues Cys104, Asp105, and Asn52
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionâelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed mechanism of methanol oxidation involving residues Asp297 and Glu171, structure-activity analysis by quantum mechanics and molecular mechanics, QM/MM, selfconsistent-charge density-functional tight-binding, SCC-DFTB, and molecular dynamics, the transition state involves Glu171-CO2- as general base
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfe, Glu177 plays the role of general base catalyst
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfer
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
Diplococcus sp.
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionâelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
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a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
acetaldehyde + 2 reduced cytochrome cL
ethanol + 2 oxidizeded cytochrome cL
-
7.06% of the activity with methanol
-
-
?
butanol + 2 oxidized cytochrome cL
butanal + 2 reduced cytochrome cL
-
49.13% of the activity with methanol
-
-
?
butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
ethanol + 2 oxidized cytochrome cL
acetaldehyde + 2 reduced cytochrome cL
-
85.13% of the activity with methanol
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced cytochrome cL
methanol + 2 oxidizeded cytochrome cL
-
73.24% of the activity with methanol
-
-
?
heptanol + 2 oxidized cytochrome cL
heptanal + 2 reduced cytochrome cL
-
101.88% of the activity with methanol
-
-
?
heptanol + 2,6-dichlorophenolindophenol
heptaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
hexanol + 2 oxidized cytochrome cL
hexanal + 2 reduced cytochrome cL
-
94.10% of the activity with methanol
-
-
?
hexanol + 2,6-dichlorophenolindophenol
hexaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
methanol + NAD+
formaldehyde + NADH + H+
-
strains grow on methanol
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
octanol + 2 oxidized cytochrome cL
octanal + 2 reduced cytochrome cL
-
16.33% of the activity with methanol
-
-
?
octanol + 2,6-dichlorophenolindophenol
octaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
pentanol + 2 oxidized cytochrome cL
pentanal + 2 reduced cytochrome cL
-
67.40% of the activity with methanol
-
-
?
pentanol + 2,6-dichlorophenolindophenol
pentaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
propanol + 2 oxidized cytochrome cL
propionaldehyde + 2 reduced cytochrome cL
-
59.93% of the activity with methanol
-
-
?
propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
sorbic alcohol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
additional information
?
-
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenol indophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenolindophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenol indophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenolindophenol as a terminal acceptor
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
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-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
native enzyme with pyrroloquinoline quinone as a prosthetic group and cytochrome cL as the primary electron acceptor
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-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
native enzyme with pyrroloquinoline quinone as a prosthetic group and cytochrome cL as the primary electron acceptor
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
Diplococcus sp.
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
Diplococcus sp.
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor. Paracoccus denitrificans contains constitutive cytochrome cL, but synthesis of cytochromes c551i and c553i is induced while growing on methanol, structures, overview
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
terminal electron acceptor is cytochrome cL
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
additional information
?
-
Diplococcus sp.
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor, catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
active site structure with important disulfide bridge of Cys103-Cys104, overview
-
-
?
additional information
?
-
active site structure, the Cys103-Cys104 disulfide bridge plays a role in the electron transfer during catalysis, overview
-
-
?
additional information
?
-
MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview
-
-
?
additional information
?
-
oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
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1.1.2.7 methanol dehydrogenase (cytochrome c)
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